5loi
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5loi is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)== | |
| + | <StructureSection load='5loi' size='340' side='right'caption='[[5loi]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5loi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.153Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5loi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loi OCA], [https://pdbe.org/5loi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5loi RCSB], [https://www.ebi.ac.uk/pdbsum/5loi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5loi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G2QDY6_MYCTT G2QDY6_MYCTT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metabolic products and environmental factors constantly damage DNA. To protect against these insults and maintain genome integrity, cells have evolved mechanisms to repair DNA lesions. One such mechanism involves Rad3, a master kinase coordinating the DNA damage response. Rad26 is a functional subunit of the Rad3-Rad26 complex and responsible for bringing the kinase to sites of DNA damage. Here, I present the crystal structure of Rad26 and identify the elements important for recruiting Rad3. The structure suggests that Rad26 is a dimer with a conserved interface in the N-terminal part of the protein. Biochemical data shows that Rad26 uses its C-terminal domain and the flanking kinase-docking motif to bind specific HEAT repeats in Rad3. Analysis of the reconstituted Rad3-Rad26 heterotetrameric complex with electron microscopy enabled me to propose a structural model for its quaternary structure. In conclusion, these results suggest that Rad26 exists as a dimer and provide crucial insight into how Rad3 is recruited and incorporated into the Rad3-Rad26 DNA repair complex. | ||
| - | + | Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.,Andersen KR J Biol Chem. 2017 Mar 17. pii: jbc.M117.780189. doi: 10.1074/jbc.M117.780189. PMID:28314775<ref>PMID:28314775</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5loi" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermothelomyces thermophilus ATCC 42464]] | ||
| + | [[Category: Andersen KR]] | ||
Current revision
Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)
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